EMD-21398

Single-particle
15.0 Å
EMD-21398 Deposition: 17/02/2020
Map released: 26/02/2020
Last modified: 14/04/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-21398

Porcine epidemic diarrhea virus (PEDV) spike protein bound to negative control polyclonal Fab

EMD-21398

Single-particle
15.0 Å
EMD-21398 Deposition: 17/02/2020
Map released: 26/02/2020
Last modified: 14/04/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Porcine epidemic diarrhea virus
Sample: Porcine epidemic diarrhea virus spike protein bound to negative control polyclonal Fab.

Deposition Authors: Kirchdoerfer RN, Martini O, Sewall LM, Bangaru S, Ward AB
Structure and immune recognition of the porcine epidemic diarrhea virus spike protein.
Kirchdoerfer RN, Bhandari M , Martini O, Sewall LM , Bangaru S , Yoon KJ, Ward AB
(2021) Structure , 29 , 385 - 392.e5
PUBMED: 33378641
DOI: doi:10.1016/j.str.2020.12.003
ISSN: 0969-2126
ASTM: STRUE6
Abstract:
Porcine epidemic diarrhea virus (PEDV) is an alphacoronavirus responsible for significant morbidity and mortality in pigs. A key determinant of viral tropism and entry, the PEDV spike protein is a key target for the host antibody response and a good candidate for a protein-based vaccine immunogen. We used electron microscopy to evaluate the PEDV spike structure, as well as pig polyclonal antibody responses to viral infection. The structure of the PEDV spike reveals a configuration similar to that of HuCoV-NL63. Several PEDV protein-protein interfaces are mediated by non-protein components, including a glycan at Asn264 and two bound palmitoleic acid molecules. The polyclonal antibody response to PEDV infection shows a dominance of epitopes in the S1 region. This structural and immune characterization provides insights into coronavirus spike stability determinants and explores the immune landscape of viral spike proteins.